Abstract
Fresh human plasma containing fibrinolytic inhibitors was incubated with traces of plasminogen-free human thrombin. Subsequently, the clottable proteins were precipitated with either 16 or 8% ethanol. N-terminal analysis demonstrated that these proteins contained more N-terminal glycine (indicating soluble fibrin) when precipitated with 16 than with 8% ethanol. This probably indicates that the presence of more than one type of soluble fibrin in thrombin-incubated plasma is not due to plasmin activity in vitro.
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